2jj4: Difference between revisions

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-{{Seed}}
-[[Image:2jj4.png|left|200px]]
-<!--
+==The complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC7942==
-The line below this paragraph, containing "STRUCTURE_2jj4", creates the "Structure Box" on the page.
+<StructureSection load='2jj4' size='340' side='right'caption='[[2jj4]], [[Resolution|resolution]] 3.46&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2jj4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JJ4 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.46&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NLG:N-ACETYL-L-GLUTAMATE'>NLG</scene></td></tr>
-{{STRUCTURE_2jj4|  PDB=2jj4  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jj4 OCA], [https://pdbe.org/2jj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jj4 RCSB], [https://www.ebi.ac.uk/pdbsum/2jj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jj4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARGB_SYNE7 ARGB_SYNE7] Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.[HAMAP-Rule:MF_00082]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/2jj4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jj4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Photosynthetic organisms can store nitrogen by synthesizing arginine, and, therefore, feedback inhibition of arginine synthesis must be relieved in these organisms when nitrogen is abundant. This relief is accomplished by the binding of the PII signal transduction protein to acetylglutamate kinase (NAGK), the controlling enzyme of arginine synthesis. Here, we describe the crystal structure of the complex between NAGK and PII of Synechococcus elongatus, at 2.75-A resolution. We prove the physiological relevance of the observed interactions by site-directed mutagenesis and functional studies. The complex consists of two polar PII trimers sandwiching one ring-like hexameric NAGK (a trimer of dimers) with the threefold axes of these molecules aligned. The binding of PII favors a narrow ring conformation of the NAGK hexamer that is associated with arginine sites having low affinity for this inhibitor. Each PII subunit contacts one NAGK subunit only. The contacts map in the inner circumference of the NAGK ring and involve two surfaces of the PII subunit. One surface is on the PII body and interacts with the C-domain of the NAGK subunit, helping widen the arginine site found on the other side of this domain. The other surface is at the distal region of a protruding large loop (T-loop) that presents a novel compact shape. This loop is inserted in the interdomain crevice of the NAGK subunit, contacting mainly the N-domain, and playing key roles in anchoring PII on NAGK, in activating NAGK, and in complex formation regulation by MgATP, ADP, 2-oxoglutarate, and by phosphorylation of serine-49.
-===THE COMPLEX OF PII AND ACETYLGLUTAMATE KINASE FROM SYNECHOCOCCUS ELONGATUS PCC7942===
+The crystal structure of the complex of PII and acetylglutamate kinase reveals how PII controls the storage of nitrogen as arginine.,Llacer JL, Contreras A, Forchhammer K, Marco-Marin C, Gil-Ortiz F, Maldonado R, Fita I, Rubio V Proc Natl Acad Sci U S A. 2007 Nov 6;104(45):17644-9. Epub 2007 Oct 24. PMID:17959776<ref>PMID:17959776</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_17959776}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2jj4" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 17959776 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17959776}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-JJ4 is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JJ4 OCA].
+[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
+[[Category: Fita I]]
-==Reference==
+[[Category: Gil-Ortiz F]]
-<ref group="xtra">PMID:17959776</ref><references group="xtra"/>
+[[Category: Llacer JL]]
-[[Category: Acetylglutamate kinase]]
+[[Category: Marco-Marin C]]
-[[Category: Synechococcus elongatus]]
+[[Category: Rubio V]]
-[[Category: Fita, I.]]
-[[Category: Gil-Ortiz, F.]]
-[[Category: Llacer, J L.]]
-[[Category: Marco-Marin, C.]]
-[[Category: Rubio, V.]]
-[[Category: Acetylglutamate]]
-[[Category: Amino-acid biosynthesis]]
-[[Category: Arginine biosynthesis]]
-[[Category: Arginine inhibition]]
-[[Category: Atp-binding]]
-[[Category: Cyanobacteria]]
-[[Category: Glnb]]
-[[Category: Hexamer]]
-[[Category: Kinase]]
-[[Category: N-acetyl-l-glutamate kinase]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphorylation]]
-[[Category: Pii signal protein]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Transferase]]
-[[Category: Trimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 01:41:06 2009''